Physical characterization of two-iron uteroferrin. Evidence for a spin-coupled binuclear iron cluster.

Antanaitis, B C; Aisen, Philip; Lilienthal, H. R.

doi:10.1016/s0021-9258(18)32844-8

Cited by 117 publications

(77 citation statements)

References 34 publications

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“…Purple acid phosphatases (PAPs) are acid metallohydrolases that contain a binuclear Fe$ + M# + centre in their active site, where M is Fe or Zn [1][2][3]. In mammals, these enzymes are also referred to as tartrate-resistant acid phosphatases (TRAPs) (EC 3.1.3.2) or type 5 acid phosphatases [4].…”

Section: Introductionmentioning

confidence: 99%

“…In humans and rats, PAP enzymes are Abbreviations used : baculo PAP, baculovirus-produced recombinant PAP ; E-64, trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane ; PAP, purple acid phosphatase ; PNPP, p-nitrophenyl phosphate ; pS, phosphoserine ; pT, phosphothreonine ; pY, phosphotyrosine ; TRAP, tartrate-resistant acid phosphatase. 1 To whom correspondence should be addressed (e-mail Goran.Andersson!impi.ki.se).…”

Section: Introductionmentioning

confidence: 99%

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Tartrate-resistant purple acid phosphatase is synthesized as a latent proenzyme and activated by cysteine proteinases

Ljusberg¹,

Ek-Rylander²,

Andersson³

1999

Biochem. J.

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Purple acid phosphatases (PAPs) are binuclear acid metallohydrolases also referred to as tartrate-resistant acid phosphatases (TRAPs) or type 5 acid phosphatases. The cDNA sequences of TRAP/PAP enzymes from different species and organs indicate that these enzymes are translated as monomeric polypeptides of approx. 35 kDa, contrasting with the predominantly two-subunit structure observed in purified enzyme preparations. In the present study we have compared certain structural and enzyme-kinetic properties of recombinant rat PAP (monomeric) with those of the native rat bone TRAP/PAP enzyme (two-subunit), and examined effects on these parameters by cleaving the monomeric recombinant PAP with the serine proteinase trypsin or the cysteine proteinases papain or cathepsin B. Cleavage with trypsin resulted in a moderate activation of the recombinant enzyme and shifted the pH optimum to a slightly more basic value (5.0-5.5). Cleavage with papain resulted in complete activation and conferred similar properties to those of the bone PAP variant with regard to pH optimum (5.5-6.0) and sensitivity to reducing agents, as well as in the sizes of the subunits. Substrate specificity studies showed that the two-subunit bone PAP was considerably more active than the monomeric recombinant rat PAP towards a variety of serine-, threonine- and tyrosine-phosphorylated substrates. Of these substrates, bovine milk osteopontin seemed to be the most readily dephosphorylated substrate. In conclusion, the results suggest that the monomeric form of PAP represent a latent proenzyme with low enzymic activity towards both tyrosine- and serine/threonine-containing phosphorylated substrates. Besides being implicated in the catabolism of the extracellular matrix, members of the cysteine proteinase family might also exert a regulatory role in degradative processes involving the PAP enzymes by converting the newly synthesized PAPs to enzymically active and microenvironmentally regulated species.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Tartrate-resistant purple acid phosphatase is synthesized as a latent proenzyme and activated by cysteine proteinases

Ljusberg¹,

Ek-Rylander²,

Andersson³

1999

Biochem. J.

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“…Diiron complexes with a variety of multidentate ligands have been intensively studied in recent years, since it is known that dinuclear iron clusters in the active sites of metalloproteins play an important role in biological systems such as haemerythrin, 1,2 R2 protein of ribonucleotide reductase, 3 methane monooxygenase, 4-6 and purple acid phosphatase. [7][8][9] The bpmp complexes drawn in Chart 1 have a µ-phenolate bis(µ-carboxylate) diiron core similar to the active centers in the metalloproteins, and it is all the more significant, for an understanding of the intramolecular electron transfer between two iron atoms in biological systems, to know the mechanism of the temperature dependence of the electron transfer rate and what factors affect this rate. Mixed-valence dinuclear iron(,) complexes with a septadentate polypyridine ligand{Hbpmp = 2,6bis[bis(2-pyridylmethyl)aminomethyl]-4-methylphenol} were synthesized by Suzuki et al 10 and diiron(,) complexes with ligands which contain 1-methylimidazole instead of the pyridine groups, 11 or which have two phenol groups substituted for two of the pyridine groups, 12 were also reported.…”

mentioning

confidence: 99%

Crystal structures and Mössbauer spectra of mixed-valence dinuclear iron(II,III) complexes: detrapped valence states †

Manago¹,

Hayami²,

Oshio³

et al. 1999

J. Chem. Soc., Dalton Trans.

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“…The EPR, Mössbauer and magnetic properties of the two forms indicated that the iron centres are antiferromagnetically coupled in both oxidation states. [5][6][7][8][9] The PAPs thus belong to a class of diiron proteins 2 which includes haemerythrin, 10,11 methane monooxygenase 12, 13 and the R2 protein of ribonucleotide reductase. 14 In this class of diiron proteins, suitable crystals of PAPs have yet to be obtained for X-ray crystallographic examination.…”

mentioning

confidence: 99%

Towards a model for the oxidized form of purple acid phosphatase: crystal structure and magnetic properties of a binuclear iron(III) complex containing phosphate ligands

Yin¹,

Cheng²,

Yao³

et al. 1997

J. Chem. Soc., Dalton Trans.

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A novel binuclear iron() complex [{FeL[O 2 P(OPh) 2 ]} 2 ][ClO 4 ] 2 was synthesized and characterized by X-ray singlecrystal structure analysis, where HL is bis(benzimidazol-2-ylmethyl)(2-hydroxyethyl)amine. The crystals are triclinic, space group P1 ¯, with a = 11.523(9), b = 11.809(6), c = 13.406(4) Å, α = 68.52(4), β = 71.41(5), γ = 71.85(6)Њ and Z = 1. The structure shows that the iron() ions are bridged by the oxygen atoms of two L ligands and a phosphate ligand is terminally co-ordinated to each iron(). Magnetic susceptibility measurements in the range 4.2-300 K and subsequent calculations based on an isotropic Heisenberg model suggest antiferromagnetic coupling between the iron() ions with J = Ϫ17.5 cm Ϫ1 .

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Physical characterization of two-iron uteroferrin. Evidence for a spin-coupled binuclear iron cluster.

Cited by 117 publications

References 34 publications

Tartrate-resistant purple acid phosphatase is synthesized as a latent proenzyme and activated by cysteine proteinases

Tartrate-resistant purple acid phosphatase is synthesized as a latent proenzyme and activated by cysteine proteinases

Crystal structures and Mössbauer spectra of mixed-valence dinuclear iron(II,III) complexes: detrapped valence states †

Towards a model for the oxidized form of purple acid phosphatase: crystal structure and magnetic properties of a binuclear iron(III) complex containing phosphate ligands

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